Molecular crowding effects on the biochemical properties of amyloid β-heme, Aβ-Cu and Aβ-heme-Cu complexes.

ABSTRACT: Heme as a cofactor has been proposed to bind with β-amyloid peptide (Aβ) and the formed Aβ-heme complex exhibits enhanced peroxidase-like activity. So far, in vitro studies on the interactions between heme, Cu and Aβ have been exclusively performed in dilute solution. However, the intracellular environment is highly crowded with biomolecules. Therefore, exploring how Aβ-heme-Cu complexes behave under molecular crowding conditions is critical for understanding the mechanism of Aβ neurotoxicity in vivo. Herein, we selected PEG-200 as a crowding agent to mimic the crowded cytoplasmic environment for addressing the contributions of crowded physiological environments to the biochemical properties of Aβ-heme, Aβ-Cu and Aβ-heme-Cu complexes. Surprisingly, experimental studies and th

SUBMITTER: Li M 

PROVIDER: S-EPMC8159413 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature